DEACT_ENTFA
ID DEACT_ENTFA Reviewed; 369 AA.
AC Q837K0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Deacetylase EF_0837;
DE EC=3.1.1.-;
GN OrderedLocusNames=EF_0837; ORFNames=I574_01240, OO5_02741;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Enterococcus faecalis V583 (Illumina only
RT assembly).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Enterococcus faecalis V583 (PacBio/Illumina hybrid
RT assembly).";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ZINC, CARBOXYLATION
RP AT LYS-152, COFACTOR, AND FUNCTION.
RX PubMed=23214420; DOI=10.1021/bi301483z;
RA Ornelas A., Korczynska M., Ragumani S., Kumaran D., Narindoshvili T.,
RA Shoichet B.K., Swaminathan S., Raushel F.M.;
RT "Functional annotation and three-dimensional structure of an incorrectly
RT annotated dihydroorotase from cog3964 in the amidohydrolase superfamily.";
RL Biochemistry 52:228-238(2013).
CC -!- FUNCTION: Esterase that can catalyze the deacetylation of acetyl-(R)-
CC mandelate, but with very low efficiency (in vitro).
CC {ECO:0000269|PubMed:23214420}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:23214420};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:23214420};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Atu3266/EF_0837 deacetylase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016830; AAO80649.1; -; Genomic_DNA.
DR EMBL; AHYN01000012; EOT48502.1; -; Genomic_DNA.
DR EMBL; ASWP01000005; EOT88122.1; -; Genomic_DNA.
DR RefSeq; NP_814579.1; NC_004668.1.
DR RefSeq; WP_010774176.1; NZ_KE136527.1.
DR PDB; 2ICS; X-ray; 2.30 A; A=2-369.
DR PDBsum; 2ICS; -.
DR AlphaFoldDB; Q837K0; -.
DR SMR; Q837K0; -.
DR STRING; 226185.EF_0837; -.
DR EnsemblBacteria; AAO80649; AAO80649; EF_0837.
DR KEGG; efa:EF0837; -.
DR PATRIC; fig|226185.45.peg.2771; -.
DR eggNOG; COG3964; Bacteria.
DR HOGENOM; CLU_036699_1_0_9; -.
DR OMA; IGNNPPN; -.
DR EvolutionaryTrace; Q837K0; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42717; PTHR42717; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR03583; EF_0837; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..369
FT /note="Deacetylase EF_0837"
FT /id="PRO_0000429021"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23214420"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:23214420"
FT SITE 154
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:23214420"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:2ICS"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:2ICS"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 329..342
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 348..362
FT /evidence="ECO:0007829|PDB:2ICS"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2ICS"
SQ SEQUENCE 369 AA; 40658 MW; FD0F89AE680F5DC0 CRC64;
MDYDLLIKNG QTVNGMPVEI AIKEKKIAAV AATISGSAKE TIHLEPGTYV SAGWIDDHVH
CFEKMALYYD YPDEIGVKKG VTTVIDAGTT GAENIHEFYD LAQQAKTNVF GLVNISKWGI
VAQDELADLS KVQASLVKKA IQELPDFVVG IKARMSRTVI GDNGITPLEL AKQIQQENQE
IPLMVHIGSA PPHLDEILAL MEKGDVLTHC FNGKENGILD QATDKIKDFA WQAYNKGVVF
DIGHGTDSFN FHVAETALRE GMKAASISTD IYIRNRENGP VYDLATTMEK LRVVGYDWPE
IIEKVTKAPA ENFHLTQKGT LEIGKDADLT IFTIQAEEKT LTDSNGLTRV AKEQIRPIKT
IIGGQIYDN
